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P54741

- AFSK_STRCO

UniProt

P54741 - AFSK_STRCO

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Protein
Serine/threonine-protein kinase AfsK
Gene
afsK, SCO4423, SC6F11.21, SCD6.01
Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Involved in the regulation of secondary metabolism by phosphorylating, on both Ser and Thr, the AfsR global regulatory protein involved in the control of secondary metabolism.

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei44 – 441ATP By similarity
Active sitei138 – 1381Proton acceptor By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi22 – 309ATP By similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. protein serine/threonine kinase activity Source: UniProtKB-KW
Complete GO annotation...

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 5998.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine/threonine-protein kinase AfsK (EC:2.7.11.1)
    Gene namesi
    Name:afsK
    Ordered Locus Names:SCO4423
    ORF Names:SC6F11.21, SCD6.01
    OrganismiStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
    Taxonomic identifieri100226 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group
    ProteomesiUP000001973: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi44 – 441K → A: No autophosphorylation. Binds KbpA. 1 Publication
    Mutagenesisi71 – 711S → A: No autophosphorylation. 1 Publication
    Mutagenesisi128 – 1281S → A: No change in autophosphorylation. 1 Publication
    Mutagenesisi168 – 1681T → A: Almost completely abolishes autophosphorylation. No enhancement of kinase activity on AfsR. Very little constitutive kinase activity. 1 Publication
    Mutagenesisi168 – 1681T → D: Almost completely abolishes autophosphorylation. No enhancement of kinase activity on AfsR. Constitutive kinase activity. 1 Publication
    Mutagenesisi168 – 1681T → E: Almost completely abolishes autophosphorylation. No enhancement of kinase activity on AfsR. Some constitutive kinase activity. 1 Publication
    Mutagenesisi170 – 1701T → D: No change in autophosphorylation. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 799799Serine/threonine-protein kinase AfsK
    PRO_0000171234Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei71 – 711Phosphoserine; by autocatalysis1 Publication
    Modified residuei168 – 1681Phosphothreonine; by autocatalysis1 Publication

    Post-translational modificationi

    Autophosphorylated mainly on threonine residues. Some phosphorylation on serine residues. Autophosphorylation on Thr-168 is the major site enhancing kinase activity towards AfsR, and is regulated though interaction with KbpA.2 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PRIDEiP54741.

    PTM databases

    PhosSiteiP1007968.

    Interactioni

    Subunit structurei

    Interacts (via the N-terminal kinase domain) with KbpA; the interaction prevents autophosphorylation of AfsK.1 Publication

    Protein-protein interaction databases

    STRINGi100226.SCO4423.

    Structurei

    3D structure databases

    ProteinModelPortaliP54741.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini16 – 271256Protein kinase
    Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi317 – 428112Pro-rich
    Add
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000033839.
    OMAiRFRMSND.
    OrthoDBiEOG6Z0Q5X.

    Family and domain databases

    Gene3Di2.140.10.10. 1 hit.
    InterProiIPR011009. Kinase-like_dom.
    IPR018391. PQQ_beta_propeller_repeat.
    IPR002372. PQQ_repeat.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR027295. Quinonprotein_ADH-like_fam.
    IPR011047. Quinonprotein_ADH-like_supfam.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00069. Pkinase. 1 hit.
    PF01011. PQQ. 3 hits.
    [Graphical view]
    SMARTiSM00564. PQQ. 9 hits.
    [Graphical view]
    SUPFAMiSSF50998. SSF50998. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEiPS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P54741-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVDQLTQHDP RRIGPFEVLG RLGAGGMGLV YLARSASGRR VAIKTVRTEL    50
    AEDQLFRVRF TREVEAARAV SGFYTAAVVD ADPRAAVPWL ATAYVPAPSL 100
    EEIVNECGPM PAQAVRWLAA GVAEALQSIH GAGLVHRDLK PSNVLVVEDG 150
    PRVIDFGIAS GVSNTRLTMT NVAVGTPAYM SPEQAKDSRS VTGASDVFSL 200
    GSMLVFAATG HPPFHGANPV ETVFMLLREG PDLEGLPDEL RPLIESCMQM 250
    EATGRPNPAD LQAQLAPHLF GSGSDDSGTA SAWLPERAVG LIEGRRNGRP 300
    AVKPATTAGG RGHGHGPSGA RAPVHAPPLP PPPAHDPVVP APPAHVPAVP 350
    APVGAPDGGP VRLPGAAVPI GPGPRVADMR AAAVAAPPPE SALAASWSRP 400
    RPGVNGADPA VPAPAPAPPE ASPAGWRPWR FRMSNDVWGT PRVAEDLVYV 450
    TSFEVHALDV ATGRRRFKTR DVAWSMAVAD GRIHASDGPT LFALDAREGA 500
    DLWRVQTDAW VYSLQADRGT VLTATRGGGV QAWEASAGQK LWEVTGAQTD 550
    FESPEAGAAL HDGTAYVWQD ARLRALDART GDERWSYPIG DAASCGGVPV 600
    RLTQAPDGYV YVAAGTRVLA LEVASGHVRW HFEAPAVFLA PPTFVPGPAV 650
    TGGGVYLADY LGTVYALDAT DGRDRWRIAT EARSSTDPVL VAAGHVHVGS 700
    GKGLYTLDAV TGTPKWRFQA GGDIVGAPAV AEGRIHFGSS DHLLYTLKAD 750
    DGRLRWKLAT GGEITGSPVV RDGIVYACSK DRCVYALDAE KGTGTARTT 799
    Length:799
    Mass (Da):83,788
    Last modified:August 14, 2001 - v2
    Checksum:i4BE9BED4169F6F5B
    GO

    Mass spectrometryi

    Molecular mass is 1638.8 Da from positions 68 - 93. Determined by ESI. 1 Publication
    Molecular mass is 1718.8 Da from positions 68 - 93. Determined by ESI. Monophosphorylated.1 Publication
    Molecular mass is 2236.5 Da from positions 117 - 137. Determined by ESI. 1 Publication
    Molecular mass is 2109.4 Da from positions 167 - 186. Determined by ESI. 1 Publication
    Molecular mass is 2189.4 Da from positions 167 - 186. Determined by ESI. Monophosphorylated.1 Publication

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D45382 Genomic DNA. Translation: BAA08229.2.
    AL939120 Genomic DNA. Translation: CAD55483.1.
    RefSeqiNP_733637.1. NC_003888.3.
    WP_011029643.1. NC_003888.3.

    Genome annotation databases

    EnsemblBacteriaiCAD55483; CAD55483; CAD55483.
    GeneIDi1099863.
    KEGGisco:SCO4423.
    PATRICi23738656. VBIStrCoe124346_4492.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D45382 Genomic DNA. Translation: BAA08229.2 .
    AL939120 Genomic DNA. Translation: CAD55483.1 .
    RefSeqi NP_733637.1. NC_003888.3.
    WP_011029643.1. NC_003888.3.

    3D structure databases

    ProteinModelPortali P54741.
    ModBasei Search...

    Protein-protein interaction databases

    STRINGi 100226.SCO4423.

    PTM databases

    PhosSitei P1007968.

    Proteomic databases

    PRIDEi P54741.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai CAD55483 ; CAD55483 ; CAD55483 .
    GeneIDi 1099863.
    KEGGi sco:SCO4423.
    PATRICi 23738656. VBIStrCoe124346_4492.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000033839.
    OMAi RFRMSND.
    OrthoDBi EOG6Z0Q5X.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 5998.

    Family and domain databases

    Gene3Di 2.140.10.10. 1 hit.
    InterProi IPR011009. Kinase-like_dom.
    IPR018391. PQQ_beta_propeller_repeat.
    IPR002372. PQQ_repeat.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR027295. Quinonprotein_ADH-like_fam.
    IPR011047. Quinonprotein_ADH-like_supfam.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00069. Pkinase. 1 hit.
    PF01011. PQQ. 3 hits.
    [Graphical view ]
    SMARTi SM00564. PQQ. 9 hits.
    [Graphical view ]
    SUPFAMi SSF50998. SSF50998. 1 hit.
    SSF56112. SSF56112. 1 hit.
    PROSITEi PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00108. PROTEIN_KINASE_ST. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    « Hide 'large scale' publications
    1. "Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase."
      Matsumoto A., Hong S.K., Ishizuka H., Horinouchi S., Beppu T.
      Gene 146:47-56(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: A3(2) / NRRL B-16638.
    2. "The aerial mycelium-defective phenotype of Streptomyces griseus resulting from A-factor deficiency is suppressed by a Ser/Thr kinase of S. coelicolor A3(2)."
      Ueda K., Umeyama T., Beppu T., Horinouchi S.
      Gene 169:91-95(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: A3(2) / NRRL B-16638.
    3. Matsumoto A., Hong S., Ishizuka H., Horinouchi S., Beppu T., Umeyama T.
      Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 239-240.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC BAA-471 / A3(2) / M145.
    5. "Autophosphorylation of a bacterial serine/threonine kinase, AfsK, is inhibited by KbpA, an AfsK-binding protein."
      Umeyama T., Horinouchi S.
      J. Bacteriol. 183:5506-5512(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KBPA, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-44.
    6. "Self-activation of serine/threonine kinase AfsK on autophosphorylation at threonine-168."
      Tomono A., Mashiko M., Shimazu T., Inoue H., Nagasawa H., Yoshida M., Ohnishi Y., Horinouchi S.
      J. Antibiot. 59:117-123(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOPHOSPHORYLATION AT SER-71 AND THR-168, MASS SPECTROMETRY, MUTAGENESIS OF SER-71; SER-128; THR-168 AND THR-170.

    Entry informationi

    Entry nameiAFSK_STRCO
    AccessioniPrimary (citable) accession number: P54741
    Secondary accession number(s): Q9F365, Q9L002
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: August 14, 2001
    Last modified: September 3, 2014
    This is version 109 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

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